ID A0A3G9J1L5_9FIRM Unreviewed; 611 AA.
AC A0A3G9J1L5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN Name=dnaX {ECO:0000256|RuleBase:RU364063,
GN ECO:0000313|EMBL:BBH25077.1};
GN ORFNames=SG0102_00110 {ECO:0000313|EMBL:BBH25077.1};
OS Intestinibaculum porci.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Intestinibaculum.
OX NCBI_TaxID=2487118 {ECO:0000313|EMBL:BBH25077.1, ECO:0000313|Proteomes:UP000268059};
RN [1] {ECO:0000313|EMBL:BBH25077.1, ECO:0000313|Proteomes:UP000268059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0102 {ECO:0000313|EMBL:BBH25077.1,
RC ECO:0000313|Proteomes:UP000268059};
RA Kim J.S., Choe H., Lee Y.R., Kim K.M., Park D.S.;
RT "Novel Erysipelotrichaceae bacterium isolated from small intestine of a
RT swine.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|RuleBase:RU364063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU364063};
CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|RuleBase:RU364063}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR EMBL; AP019309; BBH25077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9J1L5; -.
DR KEGG; ebm:SG0102_00110; -.
DR InParanoid; A0A3G9J1L5; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000268059; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR004622; DNA_pol_HolB.
DR InterPro; IPR022754; DNA_pol_III_gamma-3.
DR InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02397; dnaX_nterm; 1.
DR NCBIfam; TIGR00678; holB; 1.
DR PANTHER; PTHR11669:SF0; PROTEIN STICHEL; 1.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR Pfam; PF13177; DNA_pol3_delta2; 1.
DR Pfam; PF12169; DNA_pol3_gamma3; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364063};
KW DNA replication {ECO:0000256|RuleBase:RU364063};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU364063};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000268059};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..177
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 382..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68623 MW; BFE35ACFAA384A5D CRC64;
MAYKSLYRAY RPQTFEDVSG QQAIIKTLRH AVEENRIAHA YLFCGPRGTG KTTIAKLFAK
AVNCTGDPKP CGQCENCKAI ENGMHQDVIE IDAASNNGVE QVRDLIEKVK YAPVMGKYKV
YIIDEVHMMS TGAFNALLKT LEEPPEHVIF ILATTEPHKI LPTIISRCQR FDFSRLTDEE
MIDRMKTVMQ EEGKTYEEGA LALIAKLANG GMRDALSILE QCLAYNDNHL SEEDVNSIYG
IVSLQDKISL IKVILAKDMN KALELIESMD AAGIDVKRLT YDLIDILKDV VIYKNTQNLS
ILSVLSSGYV DTIVPYITSD DALRFIDILV EATEKFARSV NPGIYFELAI LKLCNQDHNA
PQEVVETKTI PAVKPVQKAA MAQPPKVTPV QPQPSKPVTP ETPITEAPDG ELMNEEPVQE
EAPMTKVQPD AKPQFTHKAK VPVENHDDDI QVDPADIMNI LVQADRHILN NAKEKWPIIK
RYMANMNMAK AASLLSHGHP VAGCPGGLVI GFKFMPDVNA VNYYKNYKQL ASLLKEVFGE
EYCFVAIQDD EWLKMRQHFI ELKRANKLPQ PGALHLKHIE EHHEEPKLRD AQKYALDMFG
PDLVEFVEDD K
//
